Backbone makes a significant contribution to the electrostatics of α/β‐barrel proteins

The electrostatic properties of seven α/β‐barrel enzymes selected from different evolutionary families were studied: triose phosphate isomerase, fructose‐1,6‐bisphosphate aldolase, pyruvate kinase, mandelate racemase, trimethylamine dehydrogenase, glycolate oxidase, and narbonin, a protein without a...

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Bibliographic Details
Published in:	Protein science Vol. 6; no. 9; pp. 1849 - 1857
Main Authors:	Raychaudhuri, Soumya, Younas, Fayyaz, Karplus, P. Andrew, Faerman, Carlos H., Ripoll, Daniel R.
Format:	Journal Article
Language:	English
Published:	Bristol Cold Spring Harbor Laboratory Press 01-09-1997
Subjects:	Alcohol Oxidoreductases - chemistry electrostatic flux and field enzymes Enzymes - chemistry Fructose-Bisphosphate Aldolase - chemistry Globulins - chemistry Models, Molecular Oxidoreductases, N-Demethylating - chemistry Protein Folding Protein Structure, Secondary Pyruvate Kinase - chemistry Racemases and Epimerases - chemistry Static Electricity substrate charge Triose-Phosphate Isomerase - chemistry Vegetable Proteins - chemistry α/β‐barrel
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Summary:	The electrostatic properties of seven α/β‐barrel enzymes selected from different evolutionary families were studied: triose phosphate isomerase, fructose‐1,6‐bisphosphate aldolase, pyruvate kinase, mandelate racemase, trimethylamine dehydrogenase, glycolate oxidase, and narbonin, a protein without any known enzymatic activity. The backbone of the α/β‐barrel has a distinct electrostatic field pattern, which is dipolar along the barrel axis. When the side chains are included in the calculations the general effect is to modulate the electrostatic pattern so that the electrostatic field is generally enhanced and is focused into a specific area near the active site. We use the electrostatic flux through a square surface near the active site to gauge the functionally relevant magnitude of the electrostatic field. The calculations reveal that in six out of the seven cases the backbone itself contributes greater than 45% of the total flux. The substantial electrostatic contribution of the backbone correlates with the known preference of α/β‐barrel enzymes for negatively charged substrates.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0961-8368 1469-896X
DOI:	10.1002/pro.5560060905